Structure of PDB 5bkb Chain A

Receptor sequence
>5bkbA (length=289) Species: 80866 (Delftia acidovorans) [Search protein sequence]
PLSQRFERIAVQPLTGVLGAEITGVDLREPLDDSTWNEILDAFHTYQVIY
FPGQAITNEQHIAFSRRFGPVDPVPLLKSIEGYPEVQMIRREANESGRVI
GDDWHTDSTFLDAPPAAVVMRAIDVPEHGGDTGFLSMYTAWETLSPTMQA
TIEGLNVVHSATRVFGSLYQAQNRRFSNTSVKVMDVDAGDRETVHPLVVT
HPGSGRKGLYVNQVYCQRIEGMTDAESKPLLQFLYEHATRFDFTCRVRWK
KDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVGGVRPAR
3D structure
PDB5bkb Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants.
ChainA
Resolution1.582 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H111 D113 H270 R285
Catalytic site (residue number reindexed from 1) H105 D107 H264 R279
Enzyme Commision number 1.14.11.44: (R)-dichlorprop dioxygenase (2-oxoglutarate).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A H111 D113 H270 H105 D107 H264
BS02 AKG A I95 H111 D113 T138 H270 R281 R285 I89 H105 D107 T132 H264 R275 R279
BS03 FTV A L83 G107 H111 D113 S114 Y221 L77 G101 H105 D107 S108 Y215
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0031418 L-ascorbic acid binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:5bkb, PDBe:5bkb, PDBj:5bkb
PDBsum5bkb
PubMed31209034
UniProtP83310|RDPA_DELAC (R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (Gene Name=rdpA)

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